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1 SHIP-1 (Src homology [SH2] domain-containing inositol phosphatase).
2 e SopE-dependent activation of an endogenous inositol phosphatase.
3 vity, thus implicating the involvement of an inositol phosphatase.
4 2) domain-containing cytoplasmic tyrosine or inositol phosphatases.
5 (SHP) 2 and Src homology domain 2-containing inositol phosphatase 1 (SHIP-1) and internalization of I
6 EAT-2 was mediated by SH2 domain-containing inositol phosphatase 1 (SHIP-1), which was recruited via
10 ding evidence that Src homology 2 containing inositol phosphatase, an inhibitor of NF-kappaB activati
11 kines and the upregulation of SH2-containing inositol phosphatase, an inhibitor of NF-kappaB signalin
12 and expression of Src homology 2-containing inositol phosphatase and Src homology 2-containing prote
13 ember function: first, several targets of an inositol-phosphatase-dependent inhibitory signaling path
14 ortance of the tyrosine phosphatases and the inositol phosphatase differs depending on the cell type.
15 int mutations of the signature motifs in the inositol phosphatase domain abolish SHIP's ability to in
16 atic mutagenesis approach, we identified the inositol phosphatase domain of SHIP between amino acids
17 is novel protein, p150(ship) (SH2-containing inositol phosphatase), identifies a component of a new g
18 nositol phosphatase) or SHIP (SH2-containing inositol phosphatase) is a recently identified SH2 domai
19 ning inositol phosphatase-1 (SHIP-1) is a 5' inositol phosphatase known to negatively regulate the pr
22 usly identified as Src homology 2-containing inositol phosphatase, only under conditions of negative
25 me 10 or src homology 2 domain-containing 5' inositol phosphatase, phosphatases that negatively regul
26 the Dictyostelium genome called phospholipid-inositol phosphatase (PLIP), which defines a new subfami
27 ase (pBtk) and phosphorylated SH2-containing inositol phosphatase (pSHIP), are reduced and enhanced,
28 y, experiments identify up-regulation of the inositol phosphatase PTEN (phosphatase and tensin homolo
29 mmatory signaling by direct targeting of the inositol phosphatase PTEN, the signaling inhibitor SOCS1
31 le signaling enzymes and is regulated by the inositol phosphatases PTEN (phosphatase and tensin homol
32 nts of protein-tyrosine phosphatase-like myo-inositol phosphatases (PTPLPs) from the non-pathogenic b
39 resulted in enhanced phosphorylation of the inositol phosphatase SHIP, association of SHIP with Shc,
40 lving the tyrosine phosphatase SHP-1 and the inositol phosphatase SHIP-1 are required to maintain ane
42 y Fc gamma RIIa is tightly controlled by the inositol phosphatase SHIP-1, and the protein-tyrosine ph
48 ly identified as an SH2 domain containing 5'-inositol phosphatase (SHIP) and has been implicated in t
49 uggest that the receptor uses SH2-containing inositol phosphatase (SHIP) and SH2-containing phosphoty
50 current study, the effect of SH2-containing inositol phosphatase (SHIP) expression on these biologic
53 ough the Src homology 2 domain-containing 5' inositol phosphatase (SHIP) is a well-known mediator of
54 atase Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP) is phosphorylated and associ
55 de, we have found that the SH2-containing 5'-inositol phosphatase (SHIP) is phosphorylated on tyrosin
56 (PTEN) and Src homology 2 domain-containing inositol phosphatase (SHIP) negatively regulate phosphat
57 h IL-4R alpha signals Shc and SH2-containing inositol phosphatase (SHIP) phosphorylation, we could no
59 is pathway is blocked when an SH2-containing inositol phosphatase (SHIP)-dependent inhibitory recepto
61 (PTEN) and Src homology 2 domain-containing inositol phosphatase (SHIP-1), which hydrolyze PI(3,4,5)
64 bition is mediated by the recruitment of the inositol phosphatase, SHIP, to the Fc gammaRIIB1 phospho
66 d, in part, via diminished expression of the inositol phosphatase SHIP1 and increased activation of E
67 is associated with phosphorylation of the 5-inositol phosphatase SHIP1 and requires SHIP1 expression
74 atase and tensin homolog), or SH2-containing inositol phosphatase suppressed the Btk(lo) phenotype in
80 such as Fc epsilon RI, recruit tyrosine and inositol phosphatases that results in diminished calcium
82 ing hemITAM can also couple to intracellular inositol phosphatases to modulate selected functional re
83 as SKIP (skeletal muscle and kidney enriched inositol phosphatase), which is highly expressed in the
84 t study we have demonstrated that SHIP-2, an inositol phosphatase with high-level homology to SHIP-1,
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